Evidence map›Paper›PMID 31092687›Full record

ReviewEssays in biochemistry2019

Using genetically incorporated unnatural amino acids to control protein functions in mammalian cells.

Alexander R Nödling, Luke A Spear, Thomas L Williams, Louis Y P Luk, Yu-Hsuan Tsai

Open access · hybridAbstract readReview
In one paragraph

Review in Essays in biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
5.3field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

56 citing papers in PubMed, 110 citations in OpenAlex.

  1. Review
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  3. Evolutionarily conserved hydrophobicity and sterics in TM3/TM4 balance Orai1 pore opening.Protein science : a publication of the Protein Society · 2026
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  5. Chemical reviews · 2026
    Review
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  19. Review
  20. ORAI CaBiomolecules · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Alexander R NödlingSchool of Chemistry, Cardiff University, Cardiff, Wales, United Kingdom.ORCID 0000-0002-3483-6266
Luke A SpearSchool of Chemistry, Cardiff University, Cardiff, Wales, United Kingdom.
Thomas L WilliamsSchool of Chemistry, Cardiff University, Cardiff, Wales, United Kingdom.
Louis Y P LukSchool of Chemistry, Cardiff University, Cardiff, Wales, United Kingdom.ORCID 0000-0002-7864-6261
Yu-Hsuan TsaiSchool of Chemistry, Cardiff University, Cardiff, Wales, United Kingdom tsaiy5@cardiff.ac.uk.ORCID 0000-0003-0589-5088
Cardiff University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Genetic code expansion allows unnatural (non-canonical) amino acid incorporation into proteins of interest by repurposing the cellular translation machinery. The development of this technique has enabled site-specific incorporation of many structurally and chemically diverse amino acids, facilitating a plethora of applications, including protein imaging, engineering, mechanistic and structural investigations, and functional regulation. Particularly, genetic code expansion provides great tools to study mammalian proteins, of which dysregulations often have important implications in health. In recent years, a series of methods has been developed to modulate protein function through genetically incorporated unnatural amino acids. In this review, we will first discuss the basic concept of genetic code expansion and give an up-to-date list of amino acids that can be incorporated into proteins in mammalian cells. We then focus on the use of unnatural amino acids to activate, inhibit, or reversibly modulate protein function by translational, optical or chemical control. The features of each approach will also be highlighted.

Indexed as

Genetic CodeAmino AcidsAnimalsGenetic TherapyMammalsProtein EngineeringProteinsAmino AcidsProteinschemical biologygenetic code expansionprotein chemistryprotein engineeringunnatural amino acid

Identifiers

PMID31092687
PMCPMC6610526
OpenAlexW2944947741

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.